ID A0A0A5I0L5_9BACI Unreviewed; 809 AA.
AC A0A0A5I0L5;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE SubName: Full=ATP-dependent Clp protease ATP-binding protein {ECO:0000313|EMBL:KGX89387.1};
GN ORFNames=N783_06830 {ECO:0000313|EMBL:KGX89387.1};
OS Pontibacillus marinus BH030004 = DSM 16465.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Pontibacillus.
OX NCBI_TaxID=1385511 {ECO:0000313|EMBL:KGX89387.1, ECO:0000313|Proteomes:UP000030403};
RN [1] {ECO:0000313|EMBL:KGX89387.1, ECO:0000313|Proteomes:UP000030403}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BH030004 {ECO:0000313|EMBL:KGX89387.1,
RC ECO:0000313|Proteomes:UP000030403};
RA Huang J., Wang G.;
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC {ECO:0000256|RuleBase:RU004432}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KGX89387.1}.
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DR EMBL; AVPF01000016; KGX89387.1; -; Genomic_DNA.
DR RefSeq; WP_027446566.1; NZ_AVPF01000016.1.
DR AlphaFoldDB; A0A0A5I0L5; -.
DR STRING; 1385511.GCA_000425225_02915; -.
DR eggNOG; COG0542; Bacteria.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000030403; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00009; AAA; 1.
DR CDD; cd19499; RecA-like_ClpB_Hsp104-like; 1.
DR Gene3D; 1.10.8.60; -; 2.
DR Gene3D; 1.10.1780.10; Clp, N-terminal domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 4.10.860.10; UVR domain; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR019489; Clp_ATPase_C.
DR InterPro; IPR036628; Clp_N_dom_sf.
DR InterPro; IPR004176; Clp_R_dom.
DR InterPro; IPR001270; ClpA/B.
DR InterPro; IPR018368; ClpA/B_CS1.
DR InterPro; IPR028299; ClpA/B_CS2.
DR InterPro; IPR041546; ClpA/ClpB_AAA_lid.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001943; UVR_dom.
DR PANTHER; PTHR11638; ATP-DEPENDENT CLP PROTEASE; 1.
DR PANTHER; PTHR11638:SF18; HEAT SHOCK PROTEIN 104; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF07724; AAA_2; 1.
DR Pfam; PF17871; AAA_lid_9; 1.
DR Pfam; PF02861; Clp_N; 2.
DR Pfam; PF10431; ClpB_D2-small; 1.
DR PRINTS; PR00300; CLPPROTEASEA.
DR SMART; SM00382; AAA; 2.
DR SMART; SM01086; ClpB_D2-small; 1.
DR SUPFAM; SSF81923; Double Clp-N motif; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS51903; CLP_R; 1.
DR PROSITE; PS00870; CLPAB_1; 1.
DR PROSITE; PS00871; CLPAB_2; 1.
DR PROSITE; PS50151; UVR; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU004432};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|RuleBase:RU004432};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000313|EMBL:KGX89387.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:KGX89387.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000030403};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}.
FT DOMAIN 3..144
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT DOMAIN 419..454
FT /note="UVR"
FT /evidence="ECO:0000259|PROSITE:PS50151"
FT REGION 145..164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 415..468
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 809 AA; 90166 MW; 4A92B21163C3F9D6 CRC64;
MMFGRFTERA QKVLALAQEE AVRLGHNNIG TEHILLGLVR EGEGIAAKAL AALGLAADKI
QEEVEQLIGS GDKVSQTIHY TPRAKKVIEL SMDEARKLGH SYVGTEHILL GLIREGEGVA
ARVLNNLGVS LNKARQQVLQ LLGSNESTSN SRGGGQASSA NTPTLDSLAR DLTTVAKEGN
IDPVIGRSEE IERVIQVLSR RTKNNPVLIG EPGVGKTAIA EGLAQQIVNN EVPEILRDKR
VMTLDMGTVV AGTKYRGEFE DRLKKVMEEI RQAGNIILFI DELHTLIGAG GAEGAIDASN
ILKPSLARGD LQCIGATTLE EYRKYIEKDA ALERRFQPIQ VDEPTNEESE QILQGLRDRY
EAHHRVTITD EAIKSAVKLS DRYIQDRFLP DKAIDLIDEA ASKVRLRSYT APPNLKELEQ
KLEEVRKEKD AAVQSQEFEK AASLRDNEQK LREELDKTKD EWKEQQGQEN SEVTTEDIAS
VVSTWTGVPV SKLAKDESER LLNLEEVLHD RVIGQGEAVK AISKAIRRAR SGLKDPKRPI
GSFIFLGPTG VGKTELARAL AETMFGEEDA MIRVDMSEYM EKHSTSRLVG SPPGYVGYEE
GGQLTEKVRQ KPYSVILLDE IEKAHPDVFN TLLQVLEDGR LTDSKGRTVD FRNTVIIMTS
NVGAQELKSN KYAGFTMDDS GQDYKDMKSK VMEEMKKAFR PEFLNRIDEI IVFHSLEKKH
MKDIVKLMVD QLQKRLTELE VDFSLTDAAL EKIANEGFDP EYGARPLRRS IQKNVEDLLS
EELLKESISQ GENVVIDVNK NDEFYVSSK
//